title: Intrinsic bending of microtubule protofilaments.
abstract: The complex polymerization dynamics of the microtubule (MT) plus end are closely linked to the hydrolysis of the GTP nucleotide bound to the β-tubulin. The destabilization is thought to be associated with the conformational change of the tubulin dimers from the straight conformation in the MT lattice to a curved conformation. It remains under debate whether this transformation is directly related to the nucleotide state, or a consequence of the longitudinal or lateral contacts in the MT lattice. Here, we present large-scale atomistic simulations of short tubulin protofilaments with both nucleotide states, starting from both extreme conformations. Our simulations indicate that both interdimer and intradimer contacts in both GDP and GTP-bound tubulin dimers and protofilaments in solution bend. There are no observable differences between the mesoscopic properties of the contacts in GTP and GDP-bound tubulin or the intradime and interdimer interfaces.
authors.affiliation: Department of Chemistry, James Franck Institute, and Computation Institute, University of Chicago, 5735 S. Ellis Avenue, Chicago, IL 60637, USA.
authors.forename: Andrea
authors.initials: A
authors.lastname: Grafmüller
authors.forename: Gregory A
authors.initials: GA
authors.lastname: Voth
mesh_terms: D019281:Dimerization; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D058105:Polymerization; D011487:Protein Conformation; D013816:Thermodynamics; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism
chemical_list: D014404:Tubulin; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate